A new human gene hNTKL-BP1 interacts with hPirh2

Zhang, Liping; Li, Jinjun; Wang, Chunyan; Ma, Yu; Huo, Keke

doi:10.1016/j.bbrc.2005.02.156

Cited by 22 publications

(16 citation statements)

References 10 publications

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“…phosphoprotein (3), N-terminal kinase-like proteinbinding protein 1 (NTKL-BP1) (22), and calmodulin (5). Recently, it has been reported that histone deacetylase 1 (HDAC1) and the ε-subunit of coatomer complex (ε-COP) were ubiquitylated and subsequently degraded by Pirh2 (13,14).…”

Section: Mammalian Expression Vectors and Transfectionmentioning

confidence: 99%

Pirh2 interacts with and ubiquitylates signal recognition particle receptor β subunit

et al. 2008

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Section: Mammalian Expression Vectors and Transfectionmentioning

confidence: 99%

Pirh2 interacts with and ubiquitylates signal recognition particle receptor β subunit

et al. 2008

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“…Tip60 enhances Pirh2 protein stability and alters the subcellular localization of Pirh2 (21). Another target of Pirh2 is hNTKL-BP1 (N-terminal kinase-like protein-binding protein 1), a protein that is involved in mitosis-related cellular functions through its binding of NTKL (22). Logan and colleagues (2006) have reported that human Pirh2 (hPirh2) is involved in prostate cancer cell proliferation; overexpression of hPirh2 was detected in 73 of 82 (89%) resected prostate cancers, and a strong correlation was observed between hPirh2 expression and tumor aggressiveness (23).…”

Section: Introductionmentioning

confidence: 99%

Pirh2, a Ubiquitin E3 Ligase, Inhibits p73 Transcriptional Activity by Promoting Its Ubiquitination

Zeinab

Flores

et al. 2011

Molecular Cancer Research

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p73, a homolog of the tumor suppressor p53, transactivates many p53 target genes, leading to apoptosis or cellcycle arrest. p73 has recently been reported to play an important role in tumor suppression in a mouse model. Here, we show that Pirh2 physically interacted with p73 and downregulated p73 function through its E3 ligase activity. Pirh2 promoted p73 ubiquitination in vivo and in vitro. Intriguingly, Pirh2 primarily used K63-linked chains to ubiquitinate p73 in vitro, but in vivo, Pirh2 utilized K11-, K29-, K48-, and K63-linked chains to promote p73 ubiquitination. Depletion of Pirh2 by siRNA significantly reduced the ubiquitination of p73 in p53 null cells. Ectopic expression of Pirh2 repressed p73-dependent transcriptional activity, but the levels of p73 were not decreased. We consistently showed that ablation of endogenous Pirh2 restored p73-mediated transactivational activity. We found that Pirh2 repressed p73 transcriptional activity by directly inhibiting the p73 transcript, and p73 repression by Pirh2 was required for p73-dependent transcriptional activity and G 1 arrest but not for apoptosis. This study provides evidence that the ubiquitination of p73 mediated by Pirh2 represents an important pathway for controlling the suppressive function of p73. Furthermore, the data suggest a link between the transcriptional activity of p73 and its ubiquitination. Mol Cancer Res; 9(12); 1780-90. Ó2011 AACR.

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“…Accordingly, the tat-interactive protein of 60 kD (TIP60) was necessary to bind pirh2 at N-terminal amino acids and stabilize it [1,12]. Except for wt p53, Zhang [13] found that pirh2 could interact with hNTKL-BP (human NTKL bind protein), but the biological function of this awaits further investigation.…”

Section: Discussionmentioning

confidence: 99%

Impact of siRNA targeting pirh2 on proliferation and cell cycle control of the lung adenocarcinoma cell line A549

Zhu

Jin

et al. 2007

Front. Med. China

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The aim of this study was to investigate the role of pirh2 (p53-induced RING-H2) protein in the proliferation, apoptosis and cell cycle control of the lung cancer cell line A549. Pirh2 expression was detected by immunofluorescence, Western blot analysis and real-time polymerase chain reaction (PCR). Cell proliferation was assessed by cell counting kit-8 (CCK-8). Cell cycle control and apoptosis were analyzed by flow cytometry. The results showed that pirh2 was expressed in the cytoplasm of A549 cells. The inhibition of pirh2 expression by siRNA (psiRNA-pirh2) resulted in reduced cell proliferation and increased apoptosis. In addition, the number of G0/G1 phase cells was increased but G2/M cells were not affected significantly. Taken together, the inhibition of pirh2 expression in the lung adenocarcinoma cell line A549 resulted in reduced tumor cell growth via the inhibition of cell proliferation, the activation of apoptosis and the interruption of cell cycle transition.

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A new human gene hNTKL-BP1 interacts with hPirh2

Cited by 22 publications

References 10 publications

Pirh2 interacts with and ubiquitylates signal recognition particle receptor β subunit

Pirh2 interacts with and ubiquitylates signal recognition particle receptor β subunit

Pirh2, a Ubiquitin E3 Ligase, Inhibits p73 Transcriptional Activity by Promoting Its Ubiquitination

Impact of siRNA targeting pirh2 on proliferation and cell cycle control of the lung adenocarcinoma cell line A549

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